Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Introduces a double bond at position 2 in saturated acyl-CoAs of short chain length, i.e. less than 6 carbon atoms.1 Publication

Catalytic activityi

A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.1 Publication

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Kineticsi

  1. KM=10.7 µM for butanoyl-CoA1 Publication
  2. KM=32.9 µM for pentanoyl-CoA1 Publication
  3. KM=285 µM for hexanoyl-CoA1 Publication
  1. Vmax=28.3 µmol/min/mg enzyme with butanoyl-CoA as substrate1 Publication
  2. Vmax=24.3 µmol/min/mg enzyme with pentanoyl-CoA as substrate1 Publication
  3. Vmax=8.5 µmol/min/mg enzyme with hexanoyl-CoA as substrate1 Publication

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei161Substrate; via carbonyl oxygen1 Publication1
Binding sitei297FAD1 Publication1
Active sitei392Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi152 – 161FAD1 Publication10
Nucleotide bindingi185 – 187FAD1 Publication3
Nucleotide bindingi365 – 369FAD1 Publication5
Nucleotide bindingi394 – 396FAD1 Publication3

GO - Molecular functioni

  • acyl-CoA dehydrogenase activity Source: RGD
  • butyryl-CoA dehydrogenase activity Source: RGD
  • electron carrier activity Source: GO_Central
  • fatty-acyl-CoA binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD

GO - Biological processi

  • butyrate catabolic process Source: RGD
  • fatty acid beta-oxidation Source: RGD
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  • lipid homeostasis Source: GO_Central
  • protein homotetramerization Source: RGD
  • response to glucocorticoid Source: RGD
  • response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.3.8.1. 5301.
SABIO-RKP15651.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.11 Publication)
Short name:
SCAD
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene namesi
Name:Acads
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620514. Acads.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: BHF-UCL
  • mitochondrial membrane Source: BHF-UCL
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24Mitochondrion1 PublicationAdd BLAST24
ChainiPRO_000000050125 – 412Short-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphothreonineBy similarity1
Modified residuei51N6-acetyllysine; alternateBy similarity1
Modified residuei51N6-succinyllysine; alternateBy similarity1
Modified residuei72N6-acetyllysineBy similarity1
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Modified residuei208N6-acetyllysineBy similarity1
Modified residuei262N6-acetyllysine; alternateBy similarity1
Modified residuei262N6-succinyllysine; alternateBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei306N6-acetyllysine; alternateBy similarity1
Modified residuei306N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15651.
PRIDEiP15651.

PTM databases

iPTMnetiP15651.
PhosphoSitePlusiP15651.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001177.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP15651. 1 interactor.
STRINGi10116.ENSRNOP00000001556.

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 52Combined sources17
Turni53 – 56Combined sources4
Helixi57 – 63Combined sources7
Helixi68 – 77Combined sources10
Turni78 – 80Combined sources3
Beta strandi81 – 84Combined sources4
Helixi86 – 88Combined sources3
Helixi95 – 108Combined sources14
Helixi110 – 121Combined sources12
Helixi124 – 130Combined sources7
Helixi133 – 139Combined sources7
Helixi141 – 143Combined sources3
Beta strandi144 – 147Combined sources4
Beta strandi150 – 153Combined sources4
Beta strandi159 – 162Combined sources4
Beta strandi169 – 172Combined sources4
Beta strandi174 – 187Combined sources14
Turni188 – 191Combined sources4
Beta strandi193 – 201Combined sources9
Helixi203 – 208Combined sources6
Beta strandi209 – 218Combined sources10
Beta strandi222 – 224Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi238 – 249Combined sources12
Helixi250 – 252Combined sources3
Beta strandi253 – 256Combined sources4
Helixi260 – 296Combined sources37
Beta strandi298 – 303Combined sources6
Helixi304 – 306Combined sources3
Helixi308 – 336Combined sources29
Helixi342 – 367Combined sources26
Helixi368 – 371Combined sources4
Helixi378 – 385Combined sources8
Helixi386 – 389Combined sources4
Turni390 – 392Combined sources3
Helixi395 – 410Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQIX-ray2.25A/B25-412[»]
ProteinModelPortaliP15651.
SMRiP15651.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15651.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 272Substrate binding1 Publication4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0139. Eukaryota.
COG1960. LUCA.
HOVERGENiHBG000224.
InParanoidiP15651.
KOiK00248.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE
60 70 80 90 100
KELVPIAAQL DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI
110 120 130 140 150
ALEEISRGCA STGVIMSVNN SLYLGPILKF GSSQQKQQWI TPFTNGDKIG
160 170 180 190 200
CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS
210 220 230 240 250
TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK
260 270 280 290 300
ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF
310 320 330 340 350
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL
360 370 380 390 400
AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL
410
VIAGHLLRSY RS
Length:412
Mass (Da):44,765
Last modified:November 1, 1995 - v2
Checksum:i3E4A052FC99B8E14
GO

Sequence cautioni

The sequence AAA40669 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05030 mRNA. Translation: AAA40669.1. Different initiation.
PIRiB34252.
RefSeqiNP_071957.1. NM_022512.2.
UniGeneiRn.1167.

Genome annotation databases

GeneIDi64304.
KEGGirno:64304.
UCSCiRGD:620514. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05030 mRNA. Translation: AAA40669.1. Different initiation.
PIRiB34252.
RefSeqiNP_071957.1. NM_022512.2.
UniGeneiRn.1167.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQIX-ray2.25A/B25-412[»]
ProteinModelPortaliP15651.
SMRiP15651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15651. 1 interactor.
STRINGi10116.ENSRNOP00000001556.

Chemistry databases

ChEMBLiCHEMBL2176825.

PTM databases

iPTMnetiP15651.
PhosphoSitePlusiP15651.

Proteomic databases

PaxDbiP15651.
PRIDEiP15651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64304.
KEGGirno:64304.
UCSCiRGD:620514. rat.

Organism-specific databases

CTDi35.
RGDi620514. Acads.

Phylogenomic databases

eggNOGiKOG0139. Eukaryota.
COG1960. LUCA.
HOVERGENiHBG000224.
InParanoidiP15651.
KOiK00248.

Enzyme and pathway databases

UniPathwayiUPA00660.
BRENDAi1.3.8.1. 5301.
SABIO-RKP15651.

Miscellaneous databases

EvolutionaryTraceiP15651.
PROiP15651.

Gene expression databases

BgeeiENSRNOG00000001177.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACADS_RAT
AccessioniPrimary (citable) accession number: P15651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.